ID B9WKL5_CANDC Unreviewed; 553 AA.
AC B9WKL5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00021932};
DE EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363};
GN Name=PCK1 {ECO:0000313|EMBL:CAX39563.1};
GN OrderedLocusNames=Cd36_25230 {ECO:0000313|CGD:CAL0000159872};
GN ORFNames=CD36_25230 {ECO:0000313|EMBL:CAX39563.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX39563.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX39563.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=4.1.1.49; Evidence={ECO:0000256|ARBA:ARBA00001389};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC family. {ECO:0000256|ARBA:ARBA00006052}.
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DR EMBL; FM992695; CAX39563.1; -; Genomic_DNA.
DR RefSeq; XP_002421626.1; XM_002421581.1.
DR AlphaFoldDB; B9WKL5; -.
DR GeneID; 8050038; -.
DR KEGG; cdu:CD36_25230; -.
DR CGD; CAL0000159872; Cd36_25230.
DR VEuPathDB; FungiDB:CD36_25230; -.
DR eggNOG; ENOG502QQI5; Eukaryota.
DR HOGENOM; CLU_018247_0_1_1; -.
DR OrthoDB; 3740611at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002605; Chromosome R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00484; PEPCK_ATP; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 1.
DR HAMAP; MF_00453; PEPCK_ATP; 1.
DR InterPro; IPR001272; PEP_carboxykinase_ATP.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR InterPro; IPR015994; PEPCK_ATP_CS.
DR NCBIfam; TIGR00224; pckA; 1.
DR PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR Pfam; PF01293; PEPCK_ATP; 1.
DR PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR PROSITE; PS00532; PEPCK_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Kinase {ECO:0000313|EMBL:CAX39563.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CAX39563.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:CAX39563.1};
KW Transferase {ECO:0000313|EMBL:CAX39563.1}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 61164 MW; DA40A3944DEDC42E CRC64;
MAPPTAVESS INFEGHPTIK STQDPLVQKL SLNTDTVIRH NAPPPTLYED GLLEKGTTIS
STGALMAYSG NKTGRSPKDK RIVDESTSSH NIWWGPVNKQ VDELTWKISR SRALDYLRTR
EKLFVVDAYA GWDPRYRIKV RIICARAYHA LFMTNMLIRP TEEELKNFGE PDFTIYNAGQ
FPANIHTKGM TSATSVEINF KDMEMVILGT EYAGEMKKGI FTVMFYLMPI KHKVLTLHSS
CNQGVEKGDI TLFFGLSGTG KTTLSADPHR KLIGDDEHCW SDNGVFNIEG GCYAKCLDLS
AEKEPEIFNS IKFGAILENV VYDPITKVVD YEDSSITENT RCAYPIDFIP SAKIPCLADT
HPTNIILLTC DASGVLPPVS KLTNAQVMYH FISGYTSKMA GTEEGVTEPQ ATFSACFGQP
FLVLHPMKYA QQLSDKISEH NANAWLLNTG WVGSSVARGG KRCPLKYTRA ILDAIHSGEL
SKVEYEKVPV FNFNVPKSCP GVPSDILNPT KAWTQGADSF DKEIKSLASK FAENFKTYAD
QATEEVKAAG PEA
//
